Brose, Nils

[["dc.bibliographiccitation.firstpage","741"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","Neuron"],["dc.bibliographiccitation.lastpage","754"],["dc.bibliographiccitation.volume","51"],["dc.contributor.author","Varoqueaux, Frederique"],["dc.contributor.author","Aramuni, Gayane"],["dc.contributor.author","Rawson, Randi L."],["dc.contributor.author","Mohrmann, Ralf"],["dc.contributor.author","Missler, Markus"],["dc.contributor.author","Gottmann, Kurt"],["dc.contributor.author","Zhang, Weiqi"],["dc.contributor.author","Suedhof, Thomas C."],["dc.contributor.author","Brose, Nils"],["dc.date.accessioned","2017-09-07T11:52:32Z"],["dc.date.available","2017-09-07T11:52:32Z"],["dc.date.issued","2006"],["dc.description.abstract","Synaptogenesis, the generation and maturation of functional synapses between nerve cells, is an essential step in the development of neuronal networks in the brain. It is thought to be triggered by members of the neuroligin family of postsynaptic cell adhesion proteins, which may form transsynaptic contacts with presynaptic alpha- and beta-neurexins and have been implicated in the etiology of autism. We show that deletion mutant mice lacking neuroligin expression die shortly after birth due to respiratory failure. This respiratory failure is a consequence of reduced GABAergic/glycinergic and glutamatergic synaptic transmission and network activity in brainstem centers that control respiration. However, the density of synaptic contacts is not altered in neuroligin-deficient brains and cultured neurons. Our data show that neuroligins are required for proper synapse maturation and brain function, but not for the initial formation of synaptic contacts."],["dc.identifier.doi","10.1016/j.neuron.2006.09.003"],["dc.identifier.gro","3143623"],["dc.identifier.isi","000240997900013"],["dc.identifier.pmid","16982420"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1158"],["dc.notes.intern","WoS Import 2017-03-10 / Funder: NIMH NIH HHS [MH52804-08]"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Cell Press"],["dc.relation.issn","0896-6273"],["dc.title","Neuroligins determine synapse maturation and function"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","628"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","Neuron"],["dc.bibliographiccitation.lastpage","642"],["dc.bibliographiccitation.volume","63"],["dc.contributor.author","Poulopoulos, Alexandros"],["dc.contributor.author","Aramuni, Gayane"],["dc.contributor.author","Meyer, Guido"],["dc.contributor.author","Soykan, Tolga"],["dc.contributor.author","Hoon, Mrinalini"],["dc.contributor.author","Papadopoulos, Theofilos"],["dc.contributor.author","Zhang, Mingyue"],["dc.contributor.author","Paarmann, Ingo"],["dc.contributor.author","Fuchs, Celine"],["dc.contributor.author","Harvey, Kirsten"],["dc.contributor.author","Jedlicka, Peter"],["dc.contributor.author","Schwarzacher, Stephan W."],["dc.contributor.author","Betz, Heinrich"],["dc.contributor.author","Harvey, Robert J."],["dc.contributor.author","Brose, Nils"],["dc.contributor.author","Zhang, Weiqi"],["dc.contributor.author","Varoqueaux, Frederique"],["dc.date.accessioned","2017-09-07T11:46:51Z"],["dc.date.available","2017-09-07T11:46:51Z"],["dc.date.issued","2009"],["dc.description.abstract","In the mammalian CNS, each neuron typically receives thousands of synaptic inputs from diverse classes of neurons. Synaptic transmission to the postsynaptic neuron relies on localized and transmitter-specific differentiation of the plasma membrane with postsynaptic receptor, scaffolding, and adhesion proteins accumulating in precise apposition to presynaptic sites of transmitter release. We identified protein interactions of the synaptic adhesion molecule neuroligin 2 that drive postsynaptic differentiation at inhibitory synapses. Neuroligin 2 binds the scaffolding protein gephyrin through a conserved cytoplasmic motif and functions as a specific activator of collybistin, thus guiding membrane tethering of the inhibitory postsynaptic scaffold. Complexes of neuroligin 2, gephyrin and collybistin are sufficient for cell-autonomous clustering of inhibitory neurotransmitter receptors. Deletion of neuroligin 2 in mice perturbs GABAergic and glycinergic synaptic transmission and leads to a loss of postsynaptic specializations specifically at perisomatic inhibitory synapses."],["dc.identifier.doi","10.1016/j.neuron.2009.08.023"],["dc.identifier.gro","3143057"],["dc.identifier.isi","000269852300010"],["dc.identifier.pmid","19755106"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/529"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Cell Press"],["dc.relation.issn","0896-6273"],["dc.title","Neuroligin 2 Drives Postsynaptic Assembly at Perisomatic Inhibitory Synapses through Gephyrin and Collybistin"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","121"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Cell"],["dc.bibliographiccitation.lastpage","133"],["dc.bibliographiccitation.volume","108"],["dc.contributor.author","Rhee, Jeong-Seop"],["dc.contributor.author","Betz, Andrea"],["dc.contributor.author","Pyott, S."],["dc.contributor.author","Reim, Kerstin"],["dc.contributor.author","Varoqueaux, Frederique"],["dc.contributor.author","Augustin, Iris"],["dc.contributor.author","Hesse, Dörte"],["dc.contributor.author","Südhof, Thomas C."],["dc.contributor.author","Takahashi, Masami"],["dc.contributor.author","Rosenmund, Christian"],["dc.contributor.author","Brose, Nils"],["dc.date.accessioned","2017-09-07T11:45:57Z"],["dc.date.available","2017-09-07T11:45:57Z"],["dc.date.issued","2002"],["dc.description.abstract","Munc13-1 is a presynaptic protein with an essential role in synaptic vesicle priming. It contains a diacylglycerol (DAG)/beta phorbol ester binding C-1 domain and is a potential target of the DAG second messenger pathway that may act in parallel with PKCs. Using genetically modified mice that express a DAG/beta phorbol ester binding-deficient Munc13-1(H567K) variant instead of the wild-type protein, we determined the relative contribution of PKCs and Munc13-1 to DAG/beta phorbol ester-dependent regulation of neurotransmitter release. We show that Munc13s are the main presynaptic DAG/beta phorbol ester receptors in hippocampal neurons. Modulation of Munc13-1 activity by second messengers via the DAG/beta phorbol ester binding C-1 domain is essential for use-dependent alterations of synaptic efficacy and survival."],["dc.identifier.doi","10.1016/S0092-8674(01)00635-3"],["dc.identifier.gro","3144226"],["dc.identifier.isi","000173280700013"],["dc.identifier.pmid","11792326"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1827"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0092-8674"],["dc.title","β Phorbol Ester- and Diacylglycerol-Induced Augmentation of Transmitter Release Is Mediated by Munc13s and Not by PKCs"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","19538"],["dc.bibliographiccitation.issue","49"],["dc.bibliographiccitation.journal","Proceedings of the National Academy of Sciences"],["dc.bibliographiccitation.lastpage","19543"],["dc.bibliographiccitation.volume","105"],["dc.contributor.author","Cai, Haijiang"],["dc.contributor.author","Reim, Kerstin"],["dc.contributor.author","Varoqueaux, Frederique"],["dc.contributor.author","Tapechum, Sompol"],["dc.contributor.author","Hill, Kerstin"],["dc.contributor.author","Sørensen, Jakob Balslev"],["dc.contributor.author","Brose, Nils"],["dc.contributor.author","Chow, Robert H."],["dc.date.accessioned","2017-09-07T11:47:36Z"],["dc.date.available","2017-09-07T11:47:36Z"],["dc.date.issued","2008"],["dc.description.abstract","SNARE-mediated exocytosis is a multistage process central to synaptic transmission and hormone release. Complexins (CPXs) are small proteins that bind very rapidly and with a high affinity to the SNARE core complex, where they have been proposed recently to inhibit exocytosis by clamping the complex and inhibiting membrane fusion. However, several other studies also suggest that CPXs are positive regulators of neurotransmitter release. Thus, whether CPXs are positive or negative regulators of exocytosis is not known, much less the stage in the vesicle life cycle at which they function. Here, we systematically dissect the vesicle stages leading up to exocytosis using a knockout-rescue strategy in a mammalian model system. We show that adrenal chromaffin cells from CPX II knockout mice exhibit markedly diminished releasable vesicle pools (comprising the readily and slowly releasable pools), while showing no change in the kinetics of fusion pore dilation or morphological vesicle docking. Overexpression of WT CPX II-but not of SNARE-binding-deficient mutants-restores the size of the the releasable pools in knockout cells, and in WT cells it markedly enlarges them. Our results show that CPXs regulate the size of the primed vesicle pools and have a positive role in Ca²⁺-triggered exocytosis."],["dc.identifier.doi","10.1073/pnas.0810232105"],["dc.identifier.gro","3143192"],["dc.identifier.isi","000261706600091"],["dc.identifier.pmid","19033464"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/678"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Natl Acad Sciences"],["dc.relation.issn","0027-8424"],["dc.title","Complexin II plays a positive role in Ca²⁺-triggered exocytosis by facilitating vesicle priming"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","71"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Cell"],["dc.bibliographiccitation.lastpage","81"],["dc.bibliographiccitation.volume","104"],["dc.contributor.author","Reim, Kerstin"],["dc.contributor.author","Mansour, M."],["dc.contributor.author","Varoqueaux, Frederique"],["dc.contributor.author","McMahon, H. T."],["dc.contributor.author","Südhof, T. C."],["dc.contributor.author","Brose, N."],["dc.contributor.author","Rosenmund, C."],["dc.date.accessioned","2017-09-07T11:46:41Z"],["dc.date.available","2017-09-07T11:46:41Z"],["dc.date.issued","2001"],["dc.description.abstract","Synaptic vesicle fusion at synapses is triggered by increases in cytosolic Ca²⁺ levels. However, the identity of the Ca²⁺ sensor and the transduction mechanism of the Ca²⁺ trigger are unknown. We show that Complexins, stoichiometric components of the exocytotic core complex, are important regulators of transmitter release at a step immediately preceding vesicle fusion. Neurons lacking Complexins show a dramatically reduced transmitter release efficiency due to decreased Ca²⁺ sensitivity of the synaptic secretion process. Analyses of mutant neurons demonstrate that Complexins are acting at or following the Ca²⁺-triggering step of fast synchronous transmitter release by regulating the exocytotic Ca²⁺ sensor, its interaction with the core complex fusion machinery, or the efficiency of the fusion apparatus itself."],["dc.identifier.doi","10.1016/S0092-8674(01)00192-1"],["dc.identifier.gro","3144314"],["dc.identifier.isi","000166882300008"],["dc.identifier.pmid","11163241"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1925"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0092-8674"],["dc.title","Complexins regulate a late step in Ca²⁺-dependent neurotransmitter release"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","75"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Neuron"],["dc.bibliographiccitation.lastpage","88"],["dc.bibliographiccitation.volume","46"],["dc.contributor.author","Speidel, Dina"],["dc.contributor.author","Bruederle, C. E."],["dc.contributor.author","Enk, C."],["dc.contributor.author","Voets, T."],["dc.contributor.author","Varoqueaux, Frederique"],["dc.contributor.author","Reim, Kerstin"],["dc.contributor.author","Becherer, U."],["dc.contributor.author","Fornal, F"],["dc.contributor.author","Ruggieri, S."],["dc.contributor.author","Holighaus, Y"],["dc.contributor.author","Weihe, E"],["dc.contributor.author","Bruns, Dieter"],["dc.contributor.author","Brose, Nils"],["dc.contributor.author","Rettig, Jens"],["dc.date.accessioned","2017-09-07T11:54:29Z"],["dc.date.available","2017-09-07T11:54:29Z"],["dc.date.issued","2005"],["dc.description.abstract","CAPS1 is thought to play an essential role in mediating exocytosis from large dense-core vesicles (LDCVs). We generated CAPS1-deficient (KO) mice and studied exocytosis in a model system for Ca2+- dependent LDCV secretion, the adrenal chromaffin cell. Adult heterozygous CAPS1 KO cells display a gene dosage-dependent decrease of CAPS1 expression and a concomitant reduction in the number of docked vesicles and secretion. Embryonic homozygous CAPS1 KO cells show a strong reduction in the frequency of amperometrically detectable release events of transmitter-filled vesicles, while the total number of fusing vesicles, as judged by capacitance recordings or total internal reflection microscopy, remains unchanged. We conclude that CAPS1 is required for an essential step in the uptake or storage of catecholamines in LDCVs."],["dc.identifier.doi","10.1016/j.neuron.2005.02.019"],["dc.identifier.gro","3143869"],["dc.identifier.isi","000228228600010"],["dc.identifier.pmid","15820695"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1430"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0896-6273"],["dc.title","CAPS1 regulates catecholamine loading of large dense-core vesicles"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","52802"],["dc.bibliographiccitation.issue","52"],["dc.bibliographiccitation.journal","Journal of biological chemistry"],["dc.bibliographiccitation.lastpage","52809"],["dc.bibliographiccitation.volume","278"],["dc.contributor.author","Speidel, Dina"],["dc.contributor.author","Varoqueaux, Frederique"],["dc.contributor.author","Enk, C."],["dc.contributor.author","Nojiri, M."],["dc.contributor.author","Grishanin, R. N."],["dc.contributor.author","Martin, T. F. J."],["dc.contributor.author","Hofmann, K"],["dc.contributor.author","Brose, Nils"],["dc.contributor.author","Reim, Kerstin"],["dc.date.accessioned","2017-09-07T11:44:07Z"],["dc.date.available","2017-09-07T11:44:07Z"],["dc.date.issued","2003"],["dc.description.abstract","Ca²⁺-dependent activator protein for secretion (CAPS) 1 is an essential cytosolic component of the protein machinery involved in large dense-core vesicle (LDCV) exocytosis and in the secretion of a subset of neurotransmitters. In the present study, we report the identification, cloning, and comparative characterization of a second mammalian CAPS isoform, CAPS2. The structure of CAPS2 and its function in LDCV exocytosis from PC12 cells are very similar to those of CAPS1. Both isoforms are strongly expressed in neuroendocrine cells and in the brain. In subcellular fractions of the brain, both CAPS isoforms are enriched in synaptic cytosol fractions and also present on vesicular fractions. In contrast to CAPS1, which is expressed almost exclusively in brain and neuroendocrine tissues, CAPS2 is also expressed in lung, liver, and testis. Within the brain, CAPS2 expression seems to be restricted to certain brain regions and cell populations, whereas CAPS1 expression is strong in all neurons. During development, CAPS2 expression is constant between embryonic day 10 and postnatal day 60, whereas CAPS1 expression is very low before birth and increases after postnatal day 0 to reach a plateau at postnatal day 21. Light microscopic data indicate that both CAPS isoforms are specifically enriched in synaptic terminals. Ultrastructural analyses show that CAPS1 is specifically localized to glutamatergic nerve terminals. We conclude that at the functional level, CAPS2 is largely redundant with CAPS1. Differences in the spatial and temporal expression patterns of the two CAPS isoforms most likely reflect as yet unidentified subtle functional differences required in particular cell types or during a particular developmental period. The abundance of CAPS proteins in synaptic terminals indicates that they may also be important for neuronal functions that are not exclusively related to LDCV exocytosis."],["dc.identifier.doi","10.1074/jbc.M304727200"],["dc.identifier.gro","3144028"],["dc.identifier.isi","000187480700099"],["dc.identifier.pmid","14530279"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1607"],["dc.notes.intern","WoS Import 2017-03-10 / Funder: NIDDK NIH HHS [DK40428]"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0021-9258"],["dc.title","A family of Ca²⁺-dependent activator proteins for secretion. Comparative analysis of structure, expression, localization, and function"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","389"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Cell"],["dc.bibliographiccitation.lastpage","401"],["dc.bibliographiccitation.volume","118"],["dc.contributor.author","Junge, Harald J."],["dc.contributor.author","Rhee, Jeong-Seop"],["dc.contributor.author","Jahn, Olaf"],["dc.contributor.author","Varoqueaux, Frederique"],["dc.contributor.author","Spiess, Joachim"],["dc.contributor.author","Waxham, M. N."],["dc.contributor.author","Rosenmund, C."],["dc.contributor.author","Brose, Nils"],["dc.date.accessioned","2017-09-07T11:43:16Z"],["dc.date.available","2017-09-07T11:43:16Z"],["dc.date.issued","2004"],["dc.description.abstract","The efficacy of synaptic transmission between neurons can be altered transiently during neuronal network activity. This phenomenon of short-term plasticity is a key determinant of network properties; is involved in many physiological processes such as motor control, sound localization, or sensory adaptation; and is critically dependent on cytosolic [Call]. However, the underlying molecular mechanisms and the identity of the Ca²⁺ sensor/effector complexes involved are unclear. We now identify a conserved calmodulin binding site in UNC-13/Munc13s, which are essential regulators of synaptic vesicle priming and synaptic efficacy. Ca²⁺ sensor/effector complexes consisting of calmodulin and Munc13s regulate synaptic vesicle priming and synaptic efficacy in response to a residual [Ca²⁺] signal and thus shape short-term plasticity characteristics during periods of sustained synaptic activity."],["dc.identifier.doi","10.1016/j.cell.2004.06.029"],["dc.identifier.gro","3143957"],["dc.identifier.isi","000223353100014"],["dc.identifier.pmid","15294163"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1528"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0092-8674"],["dc.title","Calmodulin and Munc13 form a Ca²⁺ sensor/effector complex that controls short-term synaptic plasticity"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","449"],["dc.bibliographiccitation.issue","9"],["dc.bibliographiccitation.journal","European Journal of Cell Biology"],["dc.bibliographiccitation.lastpage","456"],["dc.bibliographiccitation.volume","83"],["dc.contributor.author","Varoqueaux, Frederique"],["dc.contributor.author","Jamain, S."],["dc.contributor.author","Brose, Nils"],["dc.date.accessioned","2017-09-07T11:43:17Z"],["dc.date.available","2017-09-07T11:43:17Z"],["dc.date.issued","2004"],["dc.description.abstract","Neuroligins are cell adhesion proteins that are thought to instruct the formation and alignment of synaptic specializations. The three known rodent neuroligin isoforms share homologous extracellular acetylcholinesterase-like domains that bridge the synaptic cleft and bind beta-neurexins. All neuroligins have identical intracellular C-terminal motifs that bind to PDZ domains of various target proteins. Neuroligin 1 is specifically localized to glutamatergic postsynaptic specializations. We show here that neuroligin 2 is exclusively localized to inhibitory synapses in rat brain and dissociated neurons. In immature neurons, neuroligin 2 is found at synapses and also at GABA(A) receptor aggregates that are not facing presynaptic termini, indicating that postsynaptic mechanisms lead to synaptic recruitment of neuroligin 2. Our findings identify neuroligin 2 as a new cell adhesion protein specific for inhibitory synapses and open new avenues for identifiying the constituents of this unique type of postsynaptic specialization."],["dc.identifier.doi","10.1078/0171-9335-00410"],["dc.identifier.gro","3143949"],["dc.identifier.isi","000224916400001"],["dc.identifier.pmid","15540461"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1519"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0171-9335"],["dc.title","Neuroligin 2 is exclusively localized to inhibitory synapses"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1143"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","The Journal of Cell Biology"],["dc.bibliographiccitation.lastpage","1161"],["dc.bibliographiccitation.volume","216"],["dc.contributor.author","Kawabe, Hiroshi"],["dc.contributor.author","Mitkovski, Miso"],["dc.contributor.author","Kaeser, Pascal S."],["dc.contributor.author","Hirrlinger, Johannes"],["dc.contributor.author","Opazo, Felipe"],["dc.contributor.author","Nestvogel, Dennis"],["dc.contributor.author","Kalla, Stefan"],["dc.contributor.author","Fejtova, Anna"],["dc.contributor.author","Verrier, Sophie E."],["dc.contributor.author","Bungers, Simon R."],["dc.contributor.author","Cooper, Benjamin H."],["dc.contributor.author","Varoqueaux, Frederique"],["dc.contributor.author","Wang, Yun"],["dc.contributor.author","Nehring, Ralf B."],["dc.contributor.author","Gundelfinger, Eckart D."],["dc.contributor.author","Rosenmund, Christian"],["dc.contributor.author","Rizzoli, Silvio O."],["dc.contributor.author","Südhof, Thomas C."],["dc.contributor.author","Rhee, Jeong-Seop"],["dc.contributor.author","Brose, Nils"],["dc.date.accessioned","2018-01-09T16:08:02Z"],["dc.date.available","2018-01-09T16:08:02Z"],["dc.date.issued","2017"],["dc.description.abstract","Presynaptic active zones (AZs) are unique subcellular structures at neuronal synapses, which contain a network of specific proteins that control synaptic vesicle (SV) tethering, priming, and fusion. Munc13s are core AZ proteins with an essential function in SV priming. In hippocampal neurons, two different Munc13s-Munc13-1 and bMunc13-2-mediate opposite forms of presynaptic short-term plasticity and thus differentially affect neuronal network characteristics. We found that most presynapses of cortical and hippocampal neurons contain only Munc13-1, whereas ∼10% contain both Munc13-1 and bMunc13-2. Whereas the presynaptic recruitment and activation of Munc13-1 depends on Rab3-interacting proteins (RIMs), we demonstrate here that bMunc13-2 is recruited to synapses by the AZ protein ELKS1, but not ELKS2, and that this recruitment determines basal SV priming and short-term plasticity. Thus, synapse-specific interactions of different Munc13 isoforms with ELKS1 or RIMs are key determinants of the molecular and functional heterogeneity of presynaptic AZs."],["dc.identifier.doi","10.1083/jcb.201606086"],["dc.identifier.pmid","28264913"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/11622"],["dc.language.iso","en"],["dc.notes.status","final"],["dc.relation.eissn","1540-8140"],["dc.relation.haserratum","/handle/2/11623"],["dc.title","ELKS1 localizes the synaptic vesicle priming protein bMunc13-2 to a specific subset of active zones"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]